[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Lai X., Shao H., Huang L.; "A thermophilic DNA ligase from Sulfolobus shibatae."; Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: This protein seals, during DNA replication, DNA recombination and DNA repair, nicks in double-stranded DNA (By similarity).
CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m).
SIMILARITY: Belongs to the ATP-dependent DNA ligase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF242877; AAF61267.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

SMR

Q9P9K9; 1-590.

ModBase

Q9P9K9.

Ontologies

GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0003910;	Molecular function: DNA ligase (ATP) activity (inferred from electronic annotation from HAMAP).
GO:0006310;	Biological process: DNA recombination (inferred from electronic annotation from HAMAP).
GO:0006281;	Biological process: DNA repair (inferred from electronic annotation from HAMAP).
GO:0006260;	Biological process: DNA replication (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00407; -; 1.
PBIL [Tree]

InterPro

IPR000977; DNA_ligase.
IPR012309; DNA_ligase_A_C.
IPR012310; DNA_ligase_A_M.
IPR012308; DNA_ligase_A_N.
IPR016059; DNA_ligase_CS.
IPR012340; NA-bd_OB-fold.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.50.140; OB_NA_bd_sub; 1.

Pfam

PF04679; DNA_ligase_A_C; 1.
PF01068; DNA_ligase_A_M; 1.
PF04675; DNA_ligase_A_N; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00574; dnl1; 1.

PROSITE

PS00697; DNA_LIGASE_A1; 1.
PS00333; DNA_LIGASE_A2; 1.
PS50160; DNA_LIGASE_A3; 1.
PROSITE graphical view of domain structure (profiles).

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Cell cycle; Cell division; DNA damage; DNA recombination; DNA repair; DNA replication; Ligase; Nucleotide-binding.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 601`	`601`	`DNA ligase.`	`PRO_0000059617`
`ACT_SITE`	`260 260`		`N6-AMP-lysine intermediate (By similarity).`

Sequence information

Length: 601 AA [This is the length of the unprocessed precursor]

Molecular weight: 67647 Da [This is the MW of the unprocessed precursor]

CRC64: C029AC84AB39AFD4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEFKVIAEYF DKLEKISSRL QLTALLADLL SKSDKAIIDK VVYIIQGKLW PDFLGYPELG 

        70         80         90        100        110        120 
IGEKFLIKAI SIATNTDENS VENLYKSTGD LGEVARRLKS KQQSTGILGF LGTSSKESLT 

       130        140        150        160        170        180 
VDEVYSTLSK VALTTGEGSR DLKIRLLAGL LKKADPLEAK FLVRFVEGRL RVGIGDATVL 

       190        200        210        220        230        240 
DAMAIAFGGG QSASEIVERA YNLRADLGNI AKIIVEKGIE ALKTLKPEVG IPIRPMLAER 

       250        260        270        280        290        300 
LSNPEEILKK VGGSALVDYK YDGERAQIHK KSDKIFIFSR RLENITSQYP DVVEYISKYV 

       310        320        330        340        350        360 
EGKEFIIEGE IVAVDPESGE MRAFQELMHR KRKSDIYEAI KEYPVNVFLF DLMYYEDVDY 

       370        380        390        400        410        420 
TTKPLEVRRK LLESIVKPND YVKIAHHIQV NNVEDLKSFF YRAISEGGEG VMVKAIGKDA 

       430        440        450        460        470        480 
IYQAGARGWL WIKLKRDYQS EMADTVDLVV VGGFYGKGKR GGKISSLLMA AYNPKTDTFE 

       490        500        510        520        530        540 
SVCKVASGFS DEQLDELQKK LMEIKRDIKH PRVNSKMEPD IWIEPVYVAE IIGAEITISP 

       550        560        570        580        590        600 
LHTCCQDVVE KDAGLSIRFP RFIRWRDDKS PEDATTTDEI LEMYNKQPKK KIESPLVDES 


V

Q9P9K9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools